5LVV

Human OGT in complex with UDP and fused substrate peptide (Tab1)

Summary for 5LVV

• Entry DOI: 10.2210/pdb5lvv/pdb
• Descriptor: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, URIDINE-5'-DIPHOSPHATE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: glycosylation, signalling, o-glcnac, o-glcnac transferase, substrate recognition, transferase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 84870.32

Authors

Raimi, O. (deposition date: 2016-09-14, release date: 2017-07-12, Last modification date: 2024-11-13)

Primary citation

Rafie, K.,Raimi, O.,Ferenbach, A.T.,Borodkin, V.S.,Kapuria, V.,van Aalten, D.M.F.
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
Open Biol, 7:-, 2017

PubMed Abstract: O-linked -acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity-signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site.

PubMed: 28659383
DOI: 10.1098/rsob.170078

Experimental method

X-RAY DIFFRACTION (2.54 Å)